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Study On The Interaction Between Fluoroquinolones And Bovine Serum Albumins By Fluorescence

Posted on:2008-01-08Degree:MasterType:Thesis
Country:ChinaCandidate:J WangFull Text:PDF
GTID:2144360218457609Subject:Inorganic Chemistry
Abstract/Summary:PDF Full Text Request
Protein palys an important role in life process,and serum albumin, which is a kind of protein and has an extensive combining ability,can bind with intrinsic and extrinsic materials,and transfer them to every parts of body.It is of current intrest in many field such as life science,clinical medicine chemisty,to explore the interaction mechanisms between these bio-macromolecules and small molecules,as well as effect of metallic ions on these reactions,at molecular level.A brief introduction is as following:1.A general introduction to the research status between proteins and drugs, and between proteins and polymers of irons,was presented.Second,the development trend and research status of fluoroquinolones was presented. Fluoroquinolones,which were newly-developed oral comprehensive antibiotics in recent years,has fairly strong flurorescent quality and therefore is used to explore the functional mechanism of drugs in human bodies,by the change of fluorescent extensity between fluoroquinolones and protein,as well as metallic irons.Finally,the research method in the paper-fluorescence method-was presented.2.The fluorescence quenching action of FLRX and BSA was much stronger in the presence of Zinc(Ⅱ),by the study of spectroscopical quality on the interaction between FLRX,BSA and Zinc(Ⅱ).According to the formula,lg((F0-F)/F)=lgK+nlg[Q],K is the binding constant,and n is the binding site.According to the slope,K=5.44×104 and n=l.05.With the concentration of Zn(Ⅱ)increasing,the combination between FLRX and BSA was enhanced,and reached to its maximum at lg[Zn(Ⅱ)]=4.5.3.The spectroscopical quality under the interaction between NFLX and BSA in the presence of Zn(Ⅱ)was studied.The change of binding constant and binding site between NFLX and BSA were also studied in presence of two different concentration of Zn(Ⅱ).Both the binding constant and binding site were increased in the presence of Zn(Ⅱ)in blood.4.Finally,the spectroscopical quality under the interaction among LMX, BSA and Cu(Ⅱ)was studied.The influence of Cu(Ⅱ)on the combination between LMX and BSA was studied as well,the binding constant between LMX and BSA was decreased in the presence of Cu(Ⅱ),consequently,the interaction between LMX and BSA weakened.5.A kind of compound SRBH,which was synthesized from rhodamine B, hydrazine hydrate and salicylaldehyde,and SRBH is non-fluorscent naturally.However,the fluorescent extensity of SRBH was enhanced more than hundredfold when the ion of Cr(VI)was added to acid solution, therefore SRBH can be tested for Cr(VI)in acid solution.It is significant for these studies to clarify the bodily transport of drugs and their functional mechanism,to clarify the molecular mechanism of interaction between drugs molecule and protein,and to know the general law of interaction between bio-macromolecules and organic mircomolecules.Also,the studies have special value for reference of designing new type of drugs.
Keywords/Search Tags:fluoroquinolone, bovine serum ablum, fluoresence quenching
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